ID   EFUD_HORCR              Reviewed;         454 AA.
AC   A0A2Z4HPY1;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=Transcription factor efuD {ECO:0000303|PubMed:30051576};
DE   AltName: Full=Enfumafungin biosynthesis cluster protein D {ECO:0000303|PubMed:30051576};
GN   Name=efuD {ECO:0000303|PubMed:30051576};
OS   Hormonema carpetanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Dothioraceae; Hormonema.
OX   NCBI_TaxID=284138;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=30051576; DOI=10.1111/1462-2920.14333;
RA   Kuhnert E., Li Y., Lan N., Yue Q., Chen L., Cox R.J., An Z., Yokoyama K.,
RA   Bills G.F.;
RT   "Enfumafungin synthase represents a novel lineage of fungal triterpene
RT   cyclases.";
RL   Environ. Microbiol. 20:3325-3342(2018).
CC   -!- FUNCTION: Transcription factor; part of the gene cluster that mediates
CC       the biosynthesis of enfumafungin, a glycosylated fernene-type
CC       triterpenoid with potent antifungal activity, mediated by its
CC       interaction with beta-1,3-glucan synthase and the fungal cell wall
CC       (PubMed:30051576). Is possibly responsible for the transcription
CC       regulation of one or more genes within the gene cluster (Probable).
CC       {ECO:0000269|PubMed:30051576, ECO:0000305|PubMed:30051576}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TFIIE alpha subunit family. {ECO:0000305}.
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DR   EMBL; MF611885; AWW17213.1; -; Genomic_DNA.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR039997; TFE.
DR   InterPro; IPR017919; TFIIE/TFIIEa_HTH.
DR   InterPro; IPR002853; TFIIE_asu.
DR   InterPro; IPR024550; TFIIEa/SarR/Rpc3_HTH_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13097; PTHR13097; 1.
DR   Pfam; PF02002; TFIIE_alpha; 1.
DR   SMART; SM00531; TFIIE; 1.
DR   PROSITE; PS51344; HTH_TFE_IIE; 1.
PE   3: Inferred from homology;
KW   Initiation factor; Nucleus; Protein biosynthesis; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..454
FT                   /note="Transcription factor efuD"
FT                   /id="PRO_0000454461"
FT   DOMAIN          4..111
FT                   /note="HTH TFE/IIEalpha-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00676"
FT   REGION          327..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..372
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..405
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..454
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  50061 MW;  574A449CDAF8DA56 CRC64;
     MDPAKELIRI TARAFYSTEH VLIIDALAIH STLNDIDLAH ILGMQLKGLR RLVGRLKEDG
     LISVESRGEK KEGAPPMTTL GKDGQPTSIK ERLFYRDWYY LNYHRAIDSI KYRMMKLSKY
     IESQGAPTTE KKDLVCPRCK SQYTELEVMD NISPMGDFLC HMCQHSLDPA TEDDTGENEN
     MKRLNDQLSR IVDIMRNIDS TDVPENDFDT ALSHALPIDR GSSNPARRIE IVESKPSIAS
     TKGLSTAPDQ ISVSVMEDGD GVKIDPEELA RRREKEAKQN MLPEWISKST ISGDITSVGA
     KEAAERASRD AHNMGLRVED VAEDKKLRTD DDGAMDSYWA ALKAEQERQA QQDQDEEEEE
     EDDDDDEFED VDVGTASAQP ASVPAISVST PATSAQVSST ATDEDGPAAK RTKVTEAQSN
     GTAPAAAASS QAAAAESKNG ESDEDEDELE FEDI